7SKT
Crystal structure of Nipah virus matrix protein
Summary for 7SKT
| Entry DOI | 10.2210/pdb7skt/pdb |
| Descriptor | Matrix protein (2 entities in total) |
| Functional Keywords | matrix, dimer, viral assembly, viral protein |
| Biological source | Nipah henipavirus |
| Total number of polymer chains | 2 |
| Total formula weight | 87922.55 |
| Authors | Norris, M.J.,Saphire, E.O. (deposition date: 2021-10-21, release date: 2022-08-24, Last modification date: 2023-10-18) |
| Primary citation | Norris, M.J.,Husby, M.L.,Kiosses, W.B.,Yin, J.,Saxena, R.,Rennick, L.J.,Heiner, A.,Harkins, S.S.,Pokhrel, R.,Schendel, S.L.,Hastie, K.M.,Landeras-Bueno, S.,Salie, Z.L.,Lee, B.,Chapagain, P.P.,Maisner, A.,Duprex, W.P.,Stahelin, R.V.,Saphire, E.O. Measles and Nipah virus assembly: Specific lipid binding drives matrix polymerization. Sci Adv, 8:eabn1440-eabn1440, 2022 Cited by PubMed Abstract: Measles virus, Nipah virus, and multiple other paramyxoviruses cause disease outbreaks in humans and animals worldwide. The paramyxovirus matrix (M) protein mediates virion assembly and budding from host cell membranes. M is thus a key target for antivirals, but few high-resolution structures of paramyxovirus M are available, and we lack the clear understanding of how viral M proteins interact with membrane lipids to mediate viral assembly and egress that is needed to guide antiviral design. Here, we reveal that M proteins associate with phosphatidylserine and phosphatidylinositol 4,5-bisphosphate [PI(4,5)P] at the plasma membrane. Using x-ray crystallography, electron microscopy, and molecular dynamics, we demonstrate that PI(4,5)P binding induces conformational and electrostatic changes in the M protein surface that trigger membrane deformation, matrix layer polymerization, and virion assembly. PubMed: 35857835DOI: 10.1126/sciadv.abn1440 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.048 Å) |
Structure validation
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